Molybdenum cofactor guanylyltransferase
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| Molybdenum cofactor guanylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.77 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Molybdenum cofactor guanylyltransferase (EC 2.7.7.77, MobA, MoCo guanylyltransferase) is an enzyme with systematic name GTP:molybdenum cofactor guanylyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction:
- GTP + molybdenum cofactor diphosphate + guanylyl molybdenum cofactor
Catalyses the guanylation of the molybdenum cofactor.
References[edit]
- ^ Lake MW, Temple CA, Rajagopalan KV, Schindelin H (December 2000). "The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis". The Journal of Biological Chemistry. 275 (51): 40211–7. doi:10.1074/jbc.m007406200. PMID 10978347.
- ^ Temple CA, Rajagopalan KV (December 2000). "Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase". The Journal of Biological Chemistry. 275 (51): 40202–10. doi:10.1074/jbc.m007407200. PMID 10978348.
- ^ Guse A, Stevenson CE, Kuper J, Buchanan G, Schwarz G, Giordano G, Magalon A, Mendel RR, Lawson DM, Palmer T (July 2003). "Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA". The Journal of Biological Chemistry. 278 (28): 25302–7. doi:10.1074/jbc.m302639200. PMID 12719427.
External links[edit]
- Molybdenum+cofactor+guanylyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
